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  The three-dimensional structure of proteasomes from Thermoplasma acidophilum as determined by electron microscopy using random conical tilting

Hegerl, R., Pfeifer, G., Pühler, G., Dahlmann, B., & Baumeister, W. (1991). The three-dimensional structure of proteasomes from Thermoplasma acidophilum as determined by electron microscopy using random conical tilting. FEBS Letters., 283(1), 117-121.

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 Creators:
Hegerl, R.1, Author              
Pfeifer, G.1, Author              
Pühler, G., Author
Dahlmann, B., Author
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: *Cysteine Endopeptidases/ch [Chemistry]; Cysteine Endopeptidases/ul [Ultrastructure]; Microscopy, Electron; *Multienzyme Complexes/ch [Chemistry]; Multienzyme Complexes/ul [Ultrastructure]; Protein Conformation; Support, Non-U.S. Gov't; *Thermoplasma/en [Enzymology]
 Abstract: The three-dimensional structure of proteasomes from the archaebacterium Thermoplasma acidophilum has been determined to a resolution of approximately 2 nm from electron micrographs of negatively stained preparations using the method of 'random conical tilting'. The particles turn out to be essentially cylinder-shaped barrels, 15 nm long and 11 nm wide, enclosing a tripartite inner compartiment. An account is given of some of the present limitations which prevent to attain a higher resolution and possible ways to overcome these limitations are indicated.

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 Dates: 1991
 Publication Status: Published in print
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 Identifiers: eDoc: 318345
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Title: FEBS Letters.
Source Genre: Journal
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Pages: - Volume / Issue: 283 (1) Sequence Number: - Start / End Page: 117 - 121 Identifier: -